This is the second renewal application of the Molecular Biophysics Training Grant at Washington University. The Molecular Biophysics Graduate Program is one of twelve Ph.D. Programs within the Division of Biology and Biomedical Sciences. Its focus on quantitative aspects of biological systems, and its requirement for significant math and physics backgrounds of its students make it unique at Washington University. The current Program Director, Dr. Kathleen Hall, has been responsible for the Program since 1997, and is expected to continue in this position for at least several more years. She is also P.I. on the Training Grant. She is assisted in administration of the Program by a steering committee of faculty and a Program coordinator in the Division office. The Program has been in place for eleven years, and has graduated twenty students with Ph.D. degrees. Our statistics show that the number of students who apply has remained relatively constant over the past five years, as has the number that matriculate. Currently, there are fifteen students in the Program, including two underrepresented minority students. There are 40 faculty members affiliated with the Program, four of whom are junior faculty. They come from seven Departments in the Medical School, and also from Biology, Chemistry, Physics, Biomedical Engineering, and the Danforth Plant Science Center. The Molecular Biophysics Graduate Program maintains a web site that lists faculty, current and past students, and events. The annual retreat, begun in 1994, joint with the Biochemistry and Bioorganic Chemistry graduate Programs, is documented on the web site. There are monthly Biophysical Evenings that showcase our faculty or introduce new developments in Biophysics; these began in 1992. Program activities are supported in part by the Division and by the Department of Biochemistry & Molecular Biophysics. There are five training positions funded by this Training Grant. Based on our admission and recruitment statistics, that number is appropriate for our Molecular Biophysics Program, and so with this renewal, we request five years of support at the level of five students per year.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Institutional National Research Service Award (T32)
Project #
5T32GM008492-15
Application #
7255599
Study Section
National Institute of General Medical Sciences Initial Review Group (BRT)
Program Officer
Flicker, Paula F
Project Start
1993-07-01
Project End
2009-06-30
Budget Start
2007-07-01
Budget End
2009-06-30
Support Year
15
Fiscal Year
2007
Total Cost
$218,839
Indirect Cost
Name
Washington University
Department
Biochemistry
Type
Schools of Medicine
DUNS #
068552207
City
Saint Louis
State
MO
Country
United States
Zip Code
63130
Maynard, Caroline M; Hall, Kathleen B (2010) Interactions between PTB RRMs induce slow motions and increase RNA binding affinity. J Mol Biol 397:260-77
Bradley, Michael J; Chivers, Peter T; Baker, Nathan A (2008) Molecular dynamics simulation of the Escherichia coli NikR protein: equilibrium conformational fluctuations reveal interdomain allosteric communication pathways. J Mol Biol 378:1155-73
Niedziela-Majka, Anita; Chesnik, Marla A; Tomko, Eric J et al. (2007) Bacillus stearothermophilus PcrA monomer is a single-stranded DNA translocase but not a processive helicase in vitro. J Biol Chem 282:27076-85
Nybakken, Grant E; Nelson, Christopher A; Chen, Beverly R et al. (2006) Crystal structure of the West Nile virus envelope glycoprotein. J Virol 80:11467-74
Bruck, Serawit; Huber, Tobias B; Ingham, Robert J et al. (2006) Identification of a novel inhibitory actin-capping protein binding motif in CD2-associated protein. J Biol Chem 281:19196-203
Wong, C Jason; Lucius, Aaron L; Lohman, Timothy M (2005) Energetics of DNA end binding by E.coli RecBC and RecBCD helicases indicate loop formation in the 3'-single-stranded DNA tail. J Mol Biol 352:765-82
Fischer, Christopher J; Maluf, Nasib K; Lohman, Timothy M (2004) Mechanism of ATP-dependent translocation of E.coli UvrD monomers along single-stranded DNA. J Mol Biol 344:1287-309
Lucius, Aaron L; Lohman, Timothy M (2004) Effects of temperature and ATP on the kinetic mechanism and kinetic step-size for E.coli RecBCD helicase-catalyzed DNA unwinding. J Mol Biol 339:751-71
Maluf, Nasib K; Lohman, Timothy M (2003) Self-association equilibria of Escherichia coli UvrD helicase studied by analytical ultracentrifugation. J Mol Biol 325:889-912
Maluf, Nasib K; Fischer, Christopher J; Lohman, Timothy M (2003) A Dimer of Escherichia coli UvrD is the active form of the helicase in vitro. J Mol Biol 325:913-35

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